Detection of the isoenzymes of wheat grain proteinase a
Phytochemistry, ISSN: 0031-9422, Vol: 45, Issue: 8, Page: 1549-1553
1997
- 8Citations
- 5Captures
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Metrics Details
- Citations8
- Citation Indexes8
- CrossRef5
- Captures5
- Readers5
Article Description
A new method for the purification of wheat cysteine proteinase A which plays a key role in the mobilization of seed storage proteins during germination has been developed. It consists of (NH 4 ) 2 SO 4 fractionation, gel filtration, and both ion-exchange and hydrophobic chromatography. Constancy of the specific activity of chromatographic fractions and their SDS-electrophoretic pattern indicates the homogeneity of the final enzyme preparation. However, electrophoresis in nondenaturing conditions revealed three protein bands of similar intensity, each showing proteolytic activity. The N-terminal sequences of all three electrophoretic components are identical. They are also identical to a segment of the amino acid sequence deduced from one of several cDNA clones derived from closely related, but non-identical mRNAs that accumulate in the aleurone layer of gibberellic acid-treated wheat [1]. It is very likely that the three electrophoretic components found are isoenzymes encoded by cDNA clones described by these authors. © 1997 Elsevier Science Ltd. All rights reserved
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S003194229700263X; http://dx.doi.org/10.1016/s0031-9422(97)00263-x; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0031213662&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/9254903; http://linkinghub.elsevier.com/retrieve/pii/S003194229700263X; http://api.elsevier.com/content/article/PII:S003194229700263X?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S003194229700263X?httpAccept=text/plain; https://linkinghub.elsevier.com/retrieve/pii/S003194229700263X; http://dx.doi.org/10.1016/s0031-9422%2897%2900263-x; https://dx.doi.org/10.1016/s0031-9422%2897%2900263-x
Elsevier BV
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